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Volumn 8, Issue 12, 1999, Pages 2734-2741

Robustness of protein folding kinetics to surface hydrophobic substitutions

Author keywords

Binary pattern; Phage display; Protein folding; Protein L; SH3 domain

Indexed keywords

IMMUNOGLOBULIN G;

EID: 0033437144     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.12.2734     Document Type: Article
Times cited : (24)

References (21)
  • 1
    • 0028802181 scopus 로고
    • Initial hydrophobic collapse in the folding of barstar
    • Agashe VR, Shastry MC, Udgaonkar JB. 1995. Initial hydrophobic collapse in the folding of barstar. Nature 377:154-157.
    • (1995) Nature , vol.377 , pp. 154-157
    • Agashe, V.R.1    Shastry, M.C.2    Udgaonkar, J.B.3
  • 2
    • 0033117763 scopus 로고    scopus 로고
    • Matching theory and experiment in protein folding
    • Alm E, Baker D. 1999a. Matching theory and experiment in protein folding. Curr Opin Struct Biol 9:189-196.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 189-196
    • Alm, E.1    Baker, D.2
  • 3
    • 0033613255 scopus 로고    scopus 로고
    • Prediction of protein folding mechanisms from free energy landscapes derived from native structures
    • Alm E, Baker D. 1999b. Prediction of protein folding mechanisms from free energy landscapes derived from native structures. Proc Natl Acad Sci USA 96:11305-11310.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11305-11310
    • Alm, E.1    Baker, D.2
  • 4
    • 0032555696 scopus 로고    scopus 로고
    • Prediction of local structure in proteins using a library of sequence-structure motifs
    • Bystroff C, Baker D. 1998. Prediction of local structure in proteins using a library of sequence-structure motifs. J Mol Biol 281:565-511.
    • (1998) J Mol Biol , vol.281 , pp. 565-1511
    • Bystroff, C.1    Baker, D.2
  • 5
    • 0033006220 scopus 로고    scopus 로고
    • Tolerance of a protein to multiple polar-to-hydrophobic surface substitutions
    • Cordes MH, Sauer RT. 1999. Tolerance of a protein to multiple polar-to-hydrophobic surface substitutions. Protein Sci 8:318-325.
    • (1999) Protein Sci , vol.8 , pp. 318-325
    • Cordes, M.H.1    Sauer, R.T.2
  • 8
    • 0000929505 scopus 로고
    • The hydrophobic moment detects periodicity in protein hydrophobicity
    • Eisenberg D, Weiss RM, Terwilliger TC. 1984. The hydrophobic moment detects periodicity in protein hydrophobicity. Proc Natl Acad Sci USA 81: 140-144.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 140-144
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 9
    • 0031444104 scopus 로고    scopus 로고
    • Folding dynamics of the Src SH3 domain
    • Grantcharova V, Baker D. 1997. Folding dynamics of the Src SH3 domain. Biochemistry 36:15685-15692.
    • (1997) Biochemistry , vol.36 , pp. 15685-15692
    • Grantcharova, V.1    Baker, D.2
  • 10
    • 0031853167 scopus 로고    scopus 로고
    • Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain
    • Grantcharova V, Riddle DS, Santiago JV, Baker D. 1998. Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain. Nat Struct Biol 5:714-720.
    • (1998) Nat Struct Biol , vol.5 , pp. 714-720
    • Grantcharova, V.1    Riddle, D.S.2    Santiago, J.V.3    Baker, D.4
  • 11
    • 0031565981 scopus 로고    scopus 로고
    • Contrasting roles for symmetrically disposed beta turns in the folding of a small protein
    • Gu H, Kim DE, Baker D. 1997. Contrasting roles for symmetrically disposed beta turns in the folding of a small protein. J Mol Biol 274:588-596.
    • (1997) J Mol Biol , vol.274 , pp. 588-596
    • Gu, H.1    Kim, D.E.2    Baker, D.3
  • 12
    • 0029004982 scopus 로고
    • A phage display system for studying the sequence determinants of protein folding
    • Gu H, Yi Q, Bray ST, Riddle DS, Shiau AK, Baker D. 1995. A phage display system for studying the sequence determinants of protein folding. Protein Sci 4:1108-1117.
    • (1995) Protein Sci , vol.4 , pp. 1108-1117
    • Gu, H.1    Yi, Q.2    Bray, S.T.3    Riddle, D.S.4    Shiau, A.K.5    Baker, D.6
  • 13
    • 0032574811 scopus 로고    scopus 로고
    • The sequences of small proteins are not extensively optimized for rapid folding by natural selection
    • Kim DE, Gu H, Baker D. 1998a. The sequences of small proteins are not extensively optimized for rapid folding by natural selection. Proc Natl Acad Sci 95:4982-4986.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 4982-4986
    • Kim, D.E.1    Gu, H.2    Baker, D.3
  • 14
    • 0032484161 scopus 로고    scopus 로고
    • The single helix in Protein L is disrupted at the rate limiting step in folding
    • Kim DE, Yi Q, Gladwin ST, Baker D. 1998b. The single helix in Protein L is disrupted at the rate limiting step in folding. J Mol Biol 284:807-815.
    • (1998) J Mol Biol , vol.284 , pp. 807-815
    • Kim, D.E.1    Yi, Q.2    Gladwin, S.T.3    Baker, D.4
  • 15
    • 0025317840 scopus 로고
    • Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface
    • Pakula AA, Sauer RT. 1990. Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface. Nature 344:363-364.
    • (1990) Nature , vol.344 , pp. 363-364
    • Pakula, A.A.1    Sauer, R.T.2
  • 16
    • 0030062459 scopus 로고    scopus 로고
    • Amino-acid substitutions in a surface turn modulate protein stability
    • Predki PF, Aagrawal V, Trunger AT, Regan L. 1996. Amino-acid substitutions in a surface turn modulate protein stability. Nat Struct Biol 3:54-58.
    • (1996) Nat Struct Biol , vol.3 , pp. 54-58
    • Predki, P.F.1    Aagrawal, V.2    Trunger, A.T.3    Regan, L.4
  • 17
    • 0030852463 scopus 로고    scopus 로고
    • Functional rapidly folding proteins from simplified amino acid sequences
    • Riddle D, Santiago J, Grantcharova V, Baker D. 1997. Functional rapidly folding proteins from simplified amino acid sequences. Nat Struct Biol 4:805-809.
    • (1997) Nat Struct Biol , vol.4 , pp. 805-809
    • Riddle, D.1    Santiago, J.2    Grantcharova, V.3    Baker, D.4
  • 18
    • 0030900533 scopus 로고    scopus 로고
    • Kinetics of folding of the IgG binding domain of peptostreptococcal protein L
    • Scalley ML, Yi Q, Gu H, McCormack A, Yates JR III, Baker D. 1997. Kinetics of folding of the IgG binding domain of peptostreptococcal protein L. Biochemistry 36:3373-3382.
    • (1997) Biochemistry , vol.36 , pp. 3373-3382
    • Scalley, M.L.1    Yi, Q.2    Gu, H.3    McCormack, A.4    Yates J.R. III5    Baker, D.6
  • 19
    • 0028792105 scopus 로고
    • Guidelines for protein design: The energetics of beta sheet side chain interactions
    • Smith CK, Regan L. 1995. Guidelines for protein design: The energetics of beta sheet side chain interactions. Science 270:980-982.
    • (1995) Science , vol.270 , pp. 980-982
    • Smith, C.K.1    Regan, L.2
  • 20
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: The rate-limiting step in two-state cytochrome c folding
    • Sosnick TR, Mayne L, Englander SW. 1996. Molecular collapse: The rate-limiting step in two-state cytochrome c folding. Proteins 24:413-426.
    • (1996) Proteins , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 21
    • 0028846974 scopus 로고
    • Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins
    • West MW, Hecht MH. 1995. Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins. Protein Sci 4:2032-2039.
    • (1995) Protein Sci , vol.4 , pp. 2032-2039
    • West, M.W.1    Hecht, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.